1f31

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(New page: 200px<br /> <applet load="1f31" size="450" color="white" frame="true" align="right" spinBox="true" caption="1f31, resolution 2.6&Aring;" /> '''CRYSTAL STRUCTURE OF...)
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Revision as of 15:08, 29 October 2007

Image:1f31.gif

1f31, resolution 2.6Å

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CRYSTAL STRUCTURE OF CLOSTRIDIUM BOTULINUM NEUROTOXIN B COMPLEXED WITH A TRISACCHARIDE

Overview

Clostridium botulinum neurotoxins are among the most potent toxins to, humans. The crystal structures of intact C. botulinum neurotoxin type B, (BoNT/B) and its complex with sialyllactose, determined at 1. 8 and 2.6 A, resolution, respectively, provide insight into its catalytic and binding, sites. The position of the belt region in BoNT/B is different from that in, BoNT/A; this observation presents interesting possibilities for designing, specific inhibitors that could be used to block the activity of this, neurotoxin. The structures of BoNT/B and its complex with sialyllactose, provide a detailed description of the active site and a model for, interactions between the toxin and its cell surface receptor. The latter, may provide valuable information for recombinant vaccine development.

About this Structure

1F31 is a [Single protein] structure of sequence from [Clostridium botulinum] with ZN and SO4 as [ligands]. Active as [[1]], with EC number [3.4.24.69]. Full crystallographic information is available from [OCA].

Reference

Structural analysis of the catalytic and binding sites of Clostridium botulinum neurotoxin B., Swaminathan S, Eswaramoorthy S, Nat Struct Biol. 2000 Aug;7(8):693-9. PMID:10932256

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